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ABSTRACT

The flavor binding behavior of native β-lactoglobuIin (β-Lg) was significantly altered by thermal or chemical modification. Upon heat-treatment at 75°C for 10 and 20 minutes the binding affinity for 2-nonanone was reduced and the number of sites for binding was increased. This was related to conformational changes and aggregation of β-Lg. Reduction of the disulfide bonds and ethylation of carboxylic acid groups also induced conformational changes which reduced the binding affinity of β-Lg for 2-nonanone.